Open AccessPurification, crystallization and preliminary crystallographic analysis of the SpaA backbone‐pilin subunit from probiotic Lactobacillus rhamnosus GG
Author(s) -
Singh Deepak,
von Ossowski Ingemar,
Palva Airi,
Krishnan Vengadesan
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113024676
Subject(s) - pilin , pilus , lactobacillus rhamnosus , crystallography , protein subunit , fimbriae proteins , recombinant dna , strain (injury) , probiotic , chemistry , resolution (logic) , biology , microbiology and biotechnology , bacteria , biochemistry , escherichia coli , anatomy , genetics , gene , artificial intelligence , computer science
Lactobacillus rhamnosus GG, a widely used Gram‐positive probiotic strain, is clinically well known for its perceived health‐promoting effects. It has recently been shown to display proteinaceous pilus fibres (called SpaCBA) on its cell surface. Structurally, SpaCBA pili possess a characteristic three‐pilin polymerized architecture, with repeating SpaA major pilins that form the backbone and two types of minor subunits (SpaB and SpaC). In this study, recombinant SpaA protein was purified, characterized and crystallized. The crystals diffracted to a resolution of 2.0 Å and belonged to space group C 2, with unit‐cell parameters a = 227.9, b = 63.2, c = 104.3 Å, β = 95.1°.